Pyrrolidonyl Peptidase in Bacteria
Pyrrolidonyl Peptidase in Bacteria
复制标题
细菌中的吡咯烷酰肽酶
DOI：
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发表时间：
1969
期刊：
影响因子：
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通讯作者：
M. Mulczyk
中科院分区：
文献类型：
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作者：
A. Szewczuk;M. Mulczyk
本文报道了1-吡咯烷酮基-α-和β-萘酰胺的合成。采用β-萘酰胺比色法测定吡咯烷酮基肽酶的活性。通过用硫酸铵沉淀，使用DEAE-纤维素柱，最后在Sephadex G-200柱上从枯草芽孢杆菌中纯化该酶。纯化的酶制剂的活性是粗匀浆的530倍。在该制剂中未发现其他肽酶活性，证明该酶可从人血清类粘蛋白中释放吡咯烷酮羧酸。结果表明，吡咯烷酮肽酶是一种SH-酶。在某些革兰氏阳性菌和革兰氏阴性菌中发现了这种酶。
The synthesis of l-pyrrolidonyl-α- and β-naphthylamides has been described. The β-naphthylamide was used for the colorimetric determination of pyrrolidonyl peptidase activity. This enzyme was purified from Bacillus subtilis by precipitation with ammonium sulphate, using a DEAE-cellulose column and finally on a Sephadex G-200 column. The activity of the purified enzyme preparation was 530-fold that of the crude homogenate. No other peptidase activity in this preparation was found. It was demonstrated that the enzyme liberates pyrrolidonecarboxylic acid from human seromucoid. The results obtained suggest that pyrrolidonyl peptidase is an SH-enzyme. The occurrence of the enzyme in some groups of gram-positive and gram-negative bacteria was noted.